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Research Article Free access | 10.1172/JCI110563

Developmental Pattern of a Serum Binding Protein for Multiplication Stimulating Activity in the Rat

Robert M. White, S. Peter Nissley, and Patricia A. Short

Endocrine Section, Metabolism Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20205

Section on Biochemistry of Cell Regulation, Laboratory of Biochemical Pharmacology, National Institute of Arthritis, Metabolism, and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20205

Pediatrics Division, Harlem Hospital, New York 10037

Find articles by White, R. in: PubMed | Google Scholar

Endocrine Section, Metabolism Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20205

Section on Biochemistry of Cell Regulation, Laboratory of Biochemical Pharmacology, National Institute of Arthritis, Metabolism, and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20205

Pediatrics Division, Harlem Hospital, New York 10037

Find articles by Nissley, S. in: PubMed | Google Scholar

Endocrine Section, Metabolism Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20205

Section on Biochemistry of Cell Regulation, Laboratory of Biochemical Pharmacology, National Institute of Arthritis, Metabolism, and Digestive Diseases, National Institutes of Health, Bethesda, Maryland 20205

Pediatrics Division, Harlem Hospital, New York 10037

Find articles by Short, P. in: PubMed | Google Scholar

Published June 1, 1982 - More info

Published in Volume 69, Issue 6 on June 1, 1982
J Clin Invest. 1982;69(6):1239–1252. https://doi.org/10.1172/JCI110563.
© 1982 The American Society for Clinical Investigation
Published June 1, 1982 - Version history
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Abstract

The concentration of multiplication stimulating activity (MSA), an insulinlike growth factor (IGF), is high in fetal rat serum. We now report that MSA is exclusively associated wth an albumin-size binding protein in fetal rat serum; the growth hormone-dependent, gamma globulin-size binding protein, which predominates in the older animal, is absent from fetal rat serum. When 125I-MSA was incubated with fetal rat serum and then gel filtered on Sephadex G-200, specific radioactivity eluted in the void volume (peak I) and the albumin region (peak III); by contrast, specific radioactivity eluted mainly in the gamma globulin region (peak II) in adult rat serum. Pools of the Sephadex G-200 fractions were chromatographed on Sephadex G-50, in 1 M acetic acid, to separate the binding protein from IGF activity. Analysis of IGF activity by chick embryo fibroblast bioassay, competitive protein binding assay, and MSA by radioimmunoassay revealed that all the IGF activity and MSA in fetal rat serum resided in peak III. Measurement of MSA binding capacity of the stripped binding protein by Scatchard analysis demonstrated that the majority of binding capacity also was found in peak III in fetal rat serum; most of MSA binding capacity was in peak II in adult rat serum. In fetal rat sera, in addition to the peak III binding protein, which is the major carrier of endogenous MSA, there is a component in peak I capable of specifically binding 125I-MSA. This component elutes as a single species from a Sepharose-6B column. As MSA associated with peak III gradually declined in early neonatal life, peak II-associated IGF activity measured by chick embryo fibroblast bioassay showed a rise of activity with a peak at 5 d of neonatal life, a nadir at 20 d, with an increase again to attain adult levels. These studies demonstrate that the MSA binding protein in the fetus is different from the growth hormone-dependent binding protein in adult life.

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